Natural metalloproteins perform many functions—ranging from sensing to electron transfer
and catalysis—in which the position and property of each ligand and metal are dictated by …

One of the hallmark advances in our understanding of metalloprotein function is showcased
in our ability to design new, non-native, catalytically active protein scaffolds. This review …

Iron–sulfur clusters have been reported to catalyze various redox transformations, including
the multielectron reduction of CO2 to hydrocarbons. Herein, we report the design and …

The ubiquity, structural variation, and functional diversity of iron-sulfur (Fe-S) clusters in
biological environments has long fascinated scientists. In nature, Fe-S clusters form a variety …

Metalloproteins are essential to sustain life. Natural evolution optimized them for intricate
structural, regulatory and catalytic functions that cannot be fulfilled by either a protein or a …

We report a sensitive colorimetric chemosensor for cysteine based on
phenylvinylbisquinoline, named M1. Selectivity for l-cysteine was demonstrated, causing a …

The genetic encoding of artificial enzymes represents a substantial advantage relative to
traditional molecular catalyst optimization, as laboratory-based directed evolution coupled …

The mutual relationship between peptides and metal ions enables metalloproteins to have
crucial roles in biological systems, including structural, sensing, electron transport, and …

This chapter presents the application of electron paramagnetic resonance (EPR)
spectroscopy to exploring the structure and dynamics of biomolecules, primarily proteins …

The highly crowded environment of the cytoplasmic spaces of living cells has considerable
effects not only on the enzymatic and binding activities, but also on the conformation and …